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1 We demonstrate that this protein is a protein methyltransferase.
2 also selective toward other AdoMet-dependent protein methyltransferases.
3 the physiological and pathological roles of protein methyltransferases.
4 can be successfully applied to Rossmann-fold protein methyltransferases.
5 probe to study the activities of endogenous protein methyltransferases.
6 ly been used to label substrates of specific protein methyltransferases.
7 m by which p53 represses gene expression via protein methyltransferases.
8 s involved in regulating this novel class of protein methyltransferases.
9 ts homologues contain motifs conserved among protein methyltransferases.
11 ut similar amounts of ADMA-producing enzyme, protein methyltransferase-1) in the human failing myocar
12 ent in Drosophila melanogaster: the arginine protein methyltransferase 5 (dPRMT5/Csul/Dart5) and its
13 s neural crest gene expression; however, the protein methyltransferases active in neural crest precur
15 activators, including CARM1 and its specific protein methyltransferase activity, in transcriptional a
18 mutations in pcm (encoding the L-isoaspartyl protein methyltransferase) and surE led to the finding t
20 roles of SETD7 in cells and further validate protein methyltransferases as a druggable target class.
21 will also be important to isolate additional protein methyltransferases by molecular cloning and to c
22 paper, we identify a class I, non-SET domain protein methyltransferase, calmodulin-lysine N-methyltra
23 ngle gene product can produce a bifunctional protein methyltransferase capable of catalyzing both (al
24 ses of coactivators: a p160 coactivator, the protein methyltransferase CARM1, and any of the three pr
26 n component, (b) CH3-H4pteridine:cob(I)amide-protein methyltransferase, catalyzed by the intact gamma
27 siae YBR261C/TAE1 gene encodes an N-terminal protein methyltransferase catalyzing the modification of
28 y of the system to stimuli is modulated by a protein methyltransferase (CheR) and a protein methylest
29 (p/CAF), as well as the recently identified protein methyltransferase, coactivator-associated argini
30 ore, we provided evidence that inhibition of protein methyltransferases, especially arginine methyltr
31 These results identify NSD3 as the first protein methyltransferase essential for neural crest gen
33 amily and facilitate the characterization of protein methyltransferase function in vivo when combined
35 apparently a consequence of a monofunctional protein methyltransferase incapable of methylating Lys-1
36 for this conserved protein and suggests that protein methyltransferases may have a role in cellular s
37 methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase (MeTr) from Clostridium thermo
38 methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase (MeTr) from Clostridium thermo
39 methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase (MeTr) from Clostridium thermo
40 ffering only in expression of the DNA repair protein methyltransferase (MGMT), a TMZ-sensitivity dete
41 a member, by sequence homology, of a nuclear protein-methyltransferase (MTase) superfamily involved i
42 he enzymes catalysing methylation reactions, protein methyltransferases (MTases), generally use S-ade
43 tides are first demethylated by a KDM, and a protein methyltransferase (PMT) is added to methylate th
45 t-translational modifications of histones by protein methyltransferases (PMTs) and histone demethylas
50 ng physiological and pathogenic functions of protein methyltransferases (PMTs) relies on knowing thei
54 ell, Yamagata et al. identify a role for the protein methyltransferase, PRMT1, in Akt-dependent regul
57 encodes ten predicted SET domain-containing protein methyltransferases, six of which have been shown
58 genetic studies suggested that a presumptive protein methyltransferase, Skb1, functions as a positive
60 ach, we identified Skb1p, a highly conserved protein methyltransferase that has been implicated previ
61 ed arginine methyltransferase 1 (CARM1) is a protein methyltransferase that negatively regulates syna
62 sferase 1 (PRMT1), another arginine-specific protein methyltransferase that shares a region of high h
63 bed in this paper, is similar to a family of protein methyltransferases that modify RNA-binding prote
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